Correction: Elongation Factor Tu and Heat Shock Protein 70 Are Membrane-Associated Proteins from Mycoplasma ovipneumoniae Capable of Inducing Strong Immune Response in Mice

Jiang, Fei; Jin-yan, HE; Navarro-Alvarez, Nalú; Xu, Jing; Li, Xia; Wu, Weiqing

doi:10.1371/journal.pone.0189562

Cited by 4 publications

(3 citation statements)

References 1 publication

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“…For example, Carrasco et al (2015) demonstrated that EF-Tu is highly immunogenic in mice infected with Borrelia burgdorferi and in Lyme disease patients. Moreover, Jiang et al (2016) suggested that EF-Tu may be a potential candidate for vaccine development against Mycoplasma ovipneumoniae infection in sheep. Recently, Widaja et al (2017) indicated that EF-Tu moonlights on the surface of bacteria are a target of proteolytic processing events and suggested that studies are needed to determine how processing generates biologically important effector molecules and if protein processing is fundamental to the expansion of protein function in bacteria belonging to different phylogenetic clades.…”

Section: Discussionmentioning

confidence: 99%

Epitope Mapping of Streptococcus agalactiae Elongation Factor Tu Protein Recognized by Human Sera

et al. 2018

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The elongation factor Tu has been identified as one of the most immunoreactive proteins that was recognized by human sera of GBS (group B streptococcus) positive patients. In this paper, we present the polypeptide-specific epitopes of the bacterial protein that are recognized by human antibodies: 28LTAAITTVLARRLP41 (peptide no. 3) and 294GQVLAKPGSINPHTKF309 (peptide no. 21). To determine the shortest amino acid sequence recognized by antibodies, truncation peptide libraries were prepared using the PEPSCAN method. The analysis of immunoreactivity of peptides with sera of GBS positive and negative women revealed that the most immunoreactive sequence was 306HTKF309. Moreover, we observed that this sequence also showed the highest specificity which was based on ratio of reactivity with sera of GBS positive relative to sera of GBS negative patients. Epitope was synthetized on Wang resin with the Fmoc strategy. Our results open the possibility to use 306HTKF309 peptide in diagnostic assays to determine Streptococcus agalactiae infection in humans.

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Section: Discussionmentioning

confidence: 99%

Epitope Mapping of Streptococcus agalactiae Elongation Factor Tu Protein Recognized by Human Sera

et al. 2018

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“…Finally, Mbov_0370 was predicted to encode a nonclassical secretory protein. A number of nonclassical secretory proteins have been identified in mycoplasmas, such as EF-Tu and DnaK in M. ovipneumoniae [52]. Several of these proteins can have moonlighting activities, such as the EF-Tu in M. hypneumoniae [53] and the TrmFO and NADH oxidase in M. bovis that were identified to be cytoadherence factors, [16,17].…”

Section: Discussionmentioning

confidence: 99%

Mbov_0503 Encodes a Novel Cytoadhesin that Facilitates Mycoplasma bovis Interaction with Tight Junctions

et al. 2020

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Molecules contributing to microbial cytoadhesion are important virulence factors. In Mycoplasma bovis, a minimal bacterium but an important cattle pathogen, binding to host cells is emerging as a complex process involving a broad range of surface-exposed structures. Here, a new cytoadhesin of M. bovis was identified by producing a collection of individual knock-out mutants and evaluating their binding to embryonic bovine lung cells. The cytoadhesive-properties of this surface-exposed protein, which is encoded by Mbov_0503 in strain HB0801, were demonstrated at both the mycoplasma cell and protein levels using confocal microscopy and ELISA. Although Mbov_0503 disruption was only associated in M. bovis with a partial reduction of its binding capacity, this moderate effect was sufficient to affect M. bovis interaction with the host-cell tight junctions, and to reduce the translocation of this mycoplasma across epithelial cell monolayers. Besides demonstrating the capacity of M. bovis to disrupt tight junctions, these results identified novel properties associated with cytoadhesin that might contribute to virulence and host colonization. These findings provide new insights into the complex interplay taking place between wall-less mycoplasmas and the host-cell surface.

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“…In chronic non-progressive pneumonia, membrane-associated proteins elongation factor Tu and Mycoplasma ovipneumoniae elongation factor HSP70 induce significant levels of cytokines, such as TNF-α, IFN-γ, IgG, IL-4, IL-5, IL-6, and IL-12 [19]. In fact, recombinant HSP70 has the potential to act as a Th1 cytokine-like adjuvant in mice [110]. A similar study has been conducted using Small HSP, that is, HSP27 as an efficient adjuvant to improve HIV-1Nef antigen-specific immunity.…”

Section: Hsp As An Adjuvant-free Carrier To Stimulate Immune Responsesmentioning

confidence: 99%

Crossroad between the Heat Shock Protein and Inflammation Pathway in Acquiring Drug Resistance: A Possible Target for Future Cancer Therapeutics

Somu,

Basavegowda,

Gomez

et al. 2023

Biomedicines

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The development of multidrug resistance (MDR) against chemotherapeutic agents has become a major impediment in cancer therapy. Understanding the underlying mechanism behind MDR can guide future treatment for cancer with better therapeutic outcomes. Recent studies evidenced that crossroads interaction between the heat shock proteins (HSP) and inflammatory responses under the tumor microenvironment plays a pivotal role in modulating drug responsiveness and drug resistance through a complex cytological process. This review aims to investigate the interrelationship between inflammation and HSP in acquiring multiple drug resistance and investigate strategies to overcome the drug resistance to improve the efficacy of cancer treatment. HSP plays a dual regulatory effect as an immunosuppressive and immunostimulatory agent, involving the simultaneous blockade of multiple signaling pathways in acquiring MDR. For example, HSP27 shows biological effects on monocytes by causing IL10 and TNFα secretion and blocking monocyte differentiation to normal dendritic cells and tumor-associated macrophages to promote cancer progression and chemoresistance. Thus, the HSP function and immune-checkpoint release modalities provide a therapeutic target for a therapeutically beneficial approach for enhancing anti-tumor immune responses. The interconnection between inflammation and HSP, along with the tumor microenvironment in acquiring drug resistance, has become crucial for rationalizing the effect of HSP immunomodulatory activity with immune checkpoint blockade. This relationship can overcome drug resistance and assist in the development of novel combinatorial cancer immunotherapy in fighting cancer with decreasing mortality rates.

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Correction: Elongation Factor Tu and Heat Shock Protein 70 Are Membrane-Associated Proteins from Mycoplasma ovipneumoniae Capable of Inducing Strong Immune Response in Mice

Cited by 4 publications

References 1 publication

Epitope Mapping of Streptococcus agalactiae Elongation Factor Tu Protein Recognized by Human Sera

Epitope Mapping of Streptococcus agalactiae Elongation Factor Tu Protein Recognized by Human Sera

Mbov_0503 Encodes a Novel Cytoadhesin that Facilitates Mycoplasma bovis Interaction with Tight Junctions

Crossroad between the Heat Shock Protein and Inflammation Pathway in Acquiring Drug Resistance: A Possible Target for Future Cancer Therapeutics

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